首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction.
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The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction.

机译:血管细胞粘附分子1(VCAM-1)的N端两个结构域片段的晶体结构:基于结构域1 C-D环的环肽可以抑制VCAM-1-alpha 4整联蛋白相互作用。

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摘要

Vascular cell adhesion molecule 1 (VCAM-1) represents a structurally and functionally distinct class of immunoglobulin superfamily molecules that bind leukocyte integrins and are involved in inflammatory and immune functions. X-ray crystallography defines the three-dimensional structure of the N-terminal two-domain fragment that participates in ligand binding. Residues in domain 1 important for ligand binding reside in the C-D loop, which projects markedly from one face of the molecule near the contact between domains 1 and 2. A cyclic peptide that mimics this loop inhibits binding of alpha 4 beta 1 integrin-bearing cells to VCAM-1. These data demonstrate how crystallographic structural information can be used to design a small molecule inhibitor of biological function.
机译:血管细胞粘附分子1(VCAM-1)代表了结构和功能上独特的一类免疫球蛋白超家族分子,它们与白细胞整联蛋白结合并参与炎症和免疫功能。 X射线晶体学定义了参与配体结合的N-末端两结构域片段的三维结构。结构域1中对配体结合重要的残基位于CD环中,该环显着从分子的一个表面突出到结构域1和2之间的接触附近。模拟该环的环肽可抑制带有α4β1整合素的细胞的结合。至VCAM-1。这些数据证明了晶体学结构信息可用于设计具有生物学功能的小分子抑制剂。

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